ID R9XC21_ASHAC Unreviewed; 1112 AA.
AC R9XC21;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=AACERI_AaceriAAR020W {ECO:0000313|EMBL:AGO10010.1};
OS Ashbya aceri (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=566037 {ECO:0000313|EMBL:AGO10010.1, ECO:0000313|Proteomes:UP000016920};
RN [1] {ECO:0000313|Proteomes:UP000016920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001556};
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DR EMBL; CP006020; AGO10010.1; -; Genomic_DNA.
DR AlphaFoldDB; R9XC21; -.
DR HOGENOM; CLU_001832_2_4_1; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000016920; Chromosome I.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008186; F:ATP-dependent activity, acting on RNA; IEA:UniProt.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0065003; P:protein-containing complex assembly; IEA:UniProt.
DR GO; GO:0022613; P:ribonucleoprotein complex biogenesis; IEA:UniProt.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd05684; S1_DHX8_helicase; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR048333; HA2_WH.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR049621; S1_DHX8_helicase.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF85; ATP-DEPENDENT RNA HELICASE DHX8; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF04408; HA2_N; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50126; S1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 183..254
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 460..623
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 645..821
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1112 AA; 126359 MW; 66CFDB84A3044897 CRC64;
MSAVEKEILN ILGINDTVVS EFVLNIYAKS DDIRSFTRQL LDLDVGIDEA RIDELYRCIE
KYEGQKSADD DANNTRSELL QLLKAELDVE DPVVAEFVFD IFSKHNSLTE FHAKLSEIDS
GLSSASIFRI HKLLRQTCAT REKTETTKAN VSGLSLPNSQ TTWDDIKGEG FREPEMELTP
LEGKIYRAVI RNIKPFGCFA RVLGTKRSCE GLIHISQLSH ERLASPNDVV SVGDHVYVKV
TKVQDNGKIS LSMKEVDQAT GQNAVVNRGR SDERIVYRRQ LTSPERWEIR QMIQSGVSSI
DDYPELKEEI SHLQQQPEQV AGNKHSNESD ELIDIELNTE HEPKFLAGQA AESRKPELPT
IVKLPKGSLN NTAMTGSKLL QEHRQEKLAL QKSTDKKERL LRELDDPEHK KRTFEDKQLA
LTAWERKRMA ERVSYGKRTN LSIKQQRESL PVFKMKQTLV DAVRDNQFLV IVGETGSGKT
TQITQYLDEE GFSARGMIGC TQPRRVAAVS VAKRVSEEMG CKLGEEVGYT IRFEDETSRK
TRIKYMTDGM LQVEALLDQA MSKYSVIMLD EAHERTVSTD VLFSLLKQAA LKRPDLRVIV
TSATLDSEKF SKYFLDCPVI KISGKTFPVE VIYSETPQLD YIEAALDTVM EIHINEGPGD
ILVFLTGQEE IDACCEILYE RVQALKDTIQ ELLILPVYSA LPSEVQSKIF EPTPKGSRKV
IFATNIAETS ITIDGIYYVV DPGYAKLNIY NPKIGIEQLV VSPISQSQAD QRKGRAGRTG
PGKCYRLFTE AAFHREMVPN SVPEIQRQNL EHTILMLKAM GINDLLNFDF MDPPPRSSMV
HALEALYNLQ ALDEDGYLTQ LGKRMSQFPM EPALSKALIA SVQEGCSDEI LTIIAMLSVQ
NVFYRPKDKA QEADNRKARF HHPFGDHLTL LNIYTRWQEN NFSKSFCAEN FLHERHLRRA
KDVKEQLKRI FKNLDLPVRS CYGNVELIRK TLVSGFFRNA AKRDPQVGYK TITDETAVSI
HPSSCLFGKE CEYVIYHSLV LTSKEYMSQV TVIDPKWLME CAPHFYKLSD PSGEKQKRLK
IVPLHNRFSK DQDSWRLSSI RQSKERALGI KR
//
